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These tails are subject to a number of publish-translational covalent modifications, together with acetylation, phosphorylation, ubiquitination, sumoylation and methylation (reviewed in 1 ). Methylation been found on a spread of lysine residues in various histones: K4 (using the one-letter amino-acid code for lysine), K9, K27, K36 and K79 in histone H3, K20 in histone H4, K59 in the globular area of histone H4 2 and K26 of histone H1B 3 A number of proteins chargeable for the methylation of particular residues have been characterised, and all but certainly one of these accommodates a SET domain